Interaction between the Chlamydia trachomatis histone H1-like protein (Hc1) and DNA.

G Christiansen; Lotte Bang Pedersen; J E Koehler; A G Lundemose; S Birkelund

Interaction between the Chlamydia trachomatis histone H1-like protein (Hc1) and DNA.

G Christiansen, Lotte Bang Pedersen, J E Koehler, A G Lundemose, S Birkelund

Cell Biology and Physiology

32 Citations (Scopus)

Abstract

The gene encoding the Chlamydia trachomatis histone H1-like protein (Hc1) from serovar L2 was cloned into Escherichia coli by use of expression vector pET11d. In this vector, transcription of the gene is under the control of a bacteriophage T7 promoter, and T7 RNA polymerase is inducible in the host. Following induction, the E. coli cells were lysed gently. Gel filtration of the lysate revealed comigration of DNA and Hc1 in the voided volume. Electron microscopy revealed the DNA to be complexed with protein in large aggregates, often in the form of spherical bodies. Purified recombinant Hc1 maintained its DNA-binding capacity and was able at high concentrations to form condensed aggregates with DNA (one molecule of Hc1 per base pair) independently of the form or size of the DNA but with a slight preference for supercoiled DNA. Hc1 alone is thus able to package DNA into condensed spherical bodies.
Udgivelsesdato: 1993-Mar

Original language	English
Journal	Journal of Bacteriology
Volume	175
Issue number	6
Pages (from-to)	1785-95
Number of pages	10
ISSN	0021-9193
Publication status	Published - 1993

Cite this

@article{9e903c30e91511dcbee902004c4f4f50,

title = "Interaction between the Chlamydia trachomatis histone H1-like protein (Hc1) and DNA.",

abstract = "The gene encoding the Chlamydia trachomatis histone H1-like protein (Hc1) from serovar L2 was cloned into Escherichia coli by use of expression vector pET11d. In this vector, transcription of the gene is under the control of a bacteriophage T7 promoter, and T7 RNA polymerase is inducible in the host. Following induction, the E. coli cells were lysed gently. Gel filtration of the lysate revealed comigration of DNA and Hc1 in the voided volume. Electron microscopy revealed the DNA to be complexed with protein in large aggregates, often in the form of spherical bodies. Purified recombinant Hc1 maintained its DNA-binding capacity and was able at high concentrations to form condensed aggregates with DNA (one molecule of Hc1 per base pair) independently of the form or size of the DNA but with a slight preference for supercoiled DNA. Hc1 alone is thus able to package DNA into condensed spherical bodies. Udgivelsesdato: 1993-Mar",

author = "G Christiansen and Pedersen, {Lotte Bang} and Koehler, {J E} and Lundemose, {A G} and S Birkelund",

note = "Keywords: Base Sequence; Chlamydia trachomatis; DNA, Bacterial; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Histones; Microscopy, Electron; Molecular Sequence Data; Protein Binding; Recombinant Proteins",

year = "1993",

language = "English",

volume = "175",

pages = "1785--95",

journal = "Journal of Bacteriology",

issn = "0021-9193",

publisher = "American Society for Microbiology",

number = "6",

}

TY - JOUR

T1 - Interaction between the Chlamydia trachomatis histone H1-like protein (Hc1) and DNA.

AU - Christiansen, G

AU - Pedersen, Lotte Bang

AU - Koehler, J E

AU - Lundemose, A G

AU - Birkelund, S

N1 - Keywords: Base Sequence; Chlamydia trachomatis; DNA, Bacterial; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Histones; Microscopy, Electron; Molecular Sequence Data; Protein Binding; Recombinant Proteins

PY - 1993

Y1 - 1993

N2 - The gene encoding the Chlamydia trachomatis histone H1-like protein (Hc1) from serovar L2 was cloned into Escherichia coli by use of expression vector pET11d. In this vector, transcription of the gene is under the control of a bacteriophage T7 promoter, and T7 RNA polymerase is inducible in the host. Following induction, the E. coli cells were lysed gently. Gel filtration of the lysate revealed comigration of DNA and Hc1 in the voided volume. Electron microscopy revealed the DNA to be complexed with protein in large aggregates, often in the form of spherical bodies. Purified recombinant Hc1 maintained its DNA-binding capacity and was able at high concentrations to form condensed aggregates with DNA (one molecule of Hc1 per base pair) independently of the form or size of the DNA but with a slight preference for supercoiled DNA. Hc1 alone is thus able to package DNA into condensed spherical bodies. Udgivelsesdato: 1993-Mar

AB - The gene encoding the Chlamydia trachomatis histone H1-like protein (Hc1) from serovar L2 was cloned into Escherichia coli by use of expression vector pET11d. In this vector, transcription of the gene is under the control of a bacteriophage T7 promoter, and T7 RNA polymerase is inducible in the host. Following induction, the E. coli cells were lysed gently. Gel filtration of the lysate revealed comigration of DNA and Hc1 in the voided volume. Electron microscopy revealed the DNA to be complexed with protein in large aggregates, often in the form of spherical bodies. Purified recombinant Hc1 maintained its DNA-binding capacity and was able at high concentrations to form condensed aggregates with DNA (one molecule of Hc1 per base pair) independently of the form or size of the DNA but with a slight preference for supercoiled DNA. Hc1 alone is thus able to package DNA into condensed spherical bodies. Udgivelsesdato: 1993-Mar

M3 - Journal article

C2 - 8449885

SN - 0021-9193

VL - 175

SP - 1785

EP - 1795

JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 6

ER -